---
title: "PRMT7 in Cancer: Biology, Mechanisms, and Emerging PRMT7-Selective Inhibitors"
id: "pubmed-42852627"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42852627"
content_type: "clinical_feed_article"
specialty: "Oncology"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42852627/"
doi: "10.3892/or.2026.9208"
published_at: "2026-10-09T12:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# PRMT7 in Cancer: Biology, Mechanisms, and Emerging PRMT7-Selective Inhibitors
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42852627
- **Specialty:** [Oncology](https://medichelpline.com/clinical-feed/oncology.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42852627/)
- **DOI:** [10.3892/or.2026.9208](https://doi.org/10.3892%2For.2026.9208)
- **Published At:** 2026-10-09T12:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- **PRMT7** is the sole type III protein arginine methyltransferase and catalyzes **arginine monomethylation**, a post‑translational modification increasingly implicated in cancer biology. - PRMT7 contributes to tumor initiation and progression via multiple molecular processes including **epigenetic regulation**, transcriptional control, RNA processing and modulation of signaling pathways. - Aberrant PRMT7 expression has been reported in diverse malignancies: leukemia, breast cancer, lung cancer, renal cell carcinoma, hepatocellular carcinoma, prostate cancer and gastric cancer. - Functionally, PRMT7 has been linked to **epithelial‑mesenchymal transition**, cancer stemness, metastasis and immune modulation; however, its effects can vary by cellular and tumor context. - The structural and biochemical properties of PRMT7—its classification as a type III PRMT and its enzymatic activity—frame its mechanistic roles and potential vulnerabilities. - PRMT7 is being evaluated as a potential therapeutic target; recent progress includes development of PRMT7‑selective compounds such as **SGC3027**, **SGC8158** and **JS1310**. - Key challenges remain for clinical translation, including defining context‑specific functions, targetable substrates, and addressing the therapeutic window and inhibitor selectivity. - Elucidating the context‑dependent roles and vulnerabilities of PRMT7 may provide opportunities for precision cancer therapy that exploit epigenetic and signaling dependencies.
## Clinical Analysis & Structured Key Points
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Epub 2026 Oct 9. # PRMT7 at the crossroads of cancer progression and therapeutic targeting (Review) [Yuchen He](https://pubmed.ncbi.nlm.nih.gov/?term=He+Y&cauthor_id=42852627)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#full-view-affiliation-1 "Department of Pharmaceutical Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Jiayi Lou](https://pubmed.ncbi.nlm.nih.gov/?term=Lou+J&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#full-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Yijing Huang](https://pubmed.ncbi.nlm.nih.gov/?term=Huang+Y&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#full-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Wen Deng](https://pubmed.ncbi.nlm.nih.gov/?term=Deng+W&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#full-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Xuehong Cai](https://pubmed.ncbi.nlm.nih.gov/?term=Cai+X&cauthor_id=42852627)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#full-view-affiliation-3 "Department of Ophthalmology, 474 Hospital of Urumqi, Urumqi, Xinjiang Uyghur Autonomous Region 830000, P.R. China.") Affiliations Expand ### Affiliations * 1 Department of Pharmaceutical Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China. * 2 Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China. * 3 Department of Ophthalmology, 474 Hospital of Urumqi, Urumqi, Xinjiang Uyghur Autonomous Region 830000, P.R. China. * PMID: **42852627** * DOI: [ 10.3892/or.2026.9208 ](https://doi.org/10.3892/or.2026.9208) Item in Clipboard Review # PRMT7 at the crossroads of cancer progression and therapeutic targeting (Review) Yuchen He et al. Oncol Rep. 2026 Dec. Show details Display options Display options Format Abstract PubMed PMID Oncol Rep Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Oncol+Rep%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22Oncol+Rep%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42852627/) . 2026 Dec;56(6):202. doi: 10.3892/or.2026.9208. Epub 2026 Oct 9. ### Authors [Yuchen He](https://pubmed.ncbi.nlm.nih.gov/?term=He+Y&cauthor_id=42852627)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#short-view-affiliation-1 "Department of Pharmaceutical Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Jiayi Lou](https://pubmed.ncbi.nlm.nih.gov/?term=Lou+J&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#short-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Yijing Huang](https://pubmed.ncbi.nlm.nih.gov/?term=Huang+Y&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#short-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Wen Deng](https://pubmed.ncbi.nlm.nih.gov/?term=Deng+W&cauthor_id=42852627)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#short-view-affiliation-2 "Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China."), [Xuehong Cai](https://pubmed.ncbi.nlm.nih.gov/?term=Cai+X&cauthor_id=42852627)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42852627/#short-view-affiliation-3 "Department of Ophthalmology, 474 Hospital of Urumqi, Urumqi, Xinjiang Uyghur Autonomous Region 830000, P.R. China.") ### Affiliations * 1 Department of Pharmaceutical Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China. * 2 Department of Food Science and Engineering, Chengdu University, Chengdu, Sichuan 610106, P.R. China. * 3 Department of Ophthalmology, 474 Hospital of Urumqi, Urumqi, Xinjiang Uyghur Autonomous Region 830000, P.R. China. * PMID: **42852627** * DOI: [ 10.3892/or.2026.9208 ](https://doi.org/10.3892/or.2026.9208) Item in Clipboard Cite Display options Display options Format Abstract PubMed PMID Linked Discoveries ## Abstract Protein arginine methyltransferase 7 (PRMT7), the sole type III PRMT family member, catalyzes arginine monomethylation and has recently emerged as an important regulator of cancer biology. Increasing evidence indicates that PRMT7 participates in tumor initiation and progression through epigenetic regulation, transcriptional control, RNA processing and signaling pathway modulation. Dysregulated PRMT7 expression has been reported in diverse malignancies, including leukemia, breast cancer, lung cancer, renal cell carcinoma, hepatocellular carcinoma, prostate cancer and gastric cancer. Functionally, PRMT7 has been implicated in epithelial‑mesenchymal transition, cancer stemness, metastasis and immune modulation, although its effects may vary depending on cellular and tumor context. The present review summarizes the structural and biochemical features of PRMT7, its mechanistic roles across different cancer types, and its potential as a therapeutic target. Recent progress in PRMT inhibitor development was also discussed, with particular emphasis on PRMT7‑selective compounds such as SGC3027, SGC8158 and JS1310, as well as the key challenges that remain for clinical translation. Elucidating the context‑specific functions and targetable vulnerabilities of PRMT7 may provide new opportunities for precision cancer therapy. **Keywords:** PRMT inhibitors; PRMT7; arginine monomethylation; cancer progression; epigenetics; tumor immunity. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Similar articles * [ Protein arginine methyltransferase 7 modulators in disease therapy: Current progress and emerged opportunity. ](https://pubmed.ncbi.nlm.nih.gov/39733511/) Yu D, Zeng L, Wang Y, Cheng B, Li D.Yu D, et al.Bioorg Chem. 2025 Jan;154:108094. doi: 10.1016/j.bioorg.2024.108094. Epub 2024 Dec 25.Bioorg Chem. 2025.PMID: 39733511Review. * [ Current and Emerging Therapies for Targeting Protein Arginine Methyltransferases (PRMTs) in Cancer. ](https://pubmed.ncbi.nlm.nih.gov/40869229/) Kaganovski A, Smith-Salzberg B, Shimshon HK, Draheim A, Spivak M, Sapir T, Shifteh D.Kaganovski A, et al.Int J Mol Sci. 2025 Aug 16;26(16):7907. doi: 10.3390/ijms26167907.Int J Mol Sci. 2025.PMID: 40869229Free PMC article.Review. * [ PRMT7 in cancer: Structure, effects, and therapeutic potentials. ](https://pubmed.ncbi.nlm.nih.gov/39615371/) Yang GJ, Liu YJ, Chen RY, Shi JJ, Li CY, Wang R, Yu J, Lu JF, Zhang LL, Yu B, Chen J.Yang GJ, et al.Eur J Med Chem. 2025 Feb 5;283:117103. doi: 10.1016/j.ejmech.2024.117103. Epub 2024 Nov 26.Eur J Med Chem. 2025.PMID: 39615371Review. * [ Structure and Function of Protein Arginine Methyltransferase PRMT7. ](https://pubmed.ncbi.nlm.nih.gov/34440512/) Halabelian L, Barsyte-Lovejoy D.Halabelian L, et al.Life (Basel). 2021 Jul 30;11(8):768. doi: 10.3390/life11080768.Life (Basel). 2021.PMID: 34440512Free PMC article.Review. * [ Protein arginine methyltransferases: promising targets for cancer therapy. ](https://pubmed.ncbi.nlm.nih.gov/34006904/) Hwang JW, Cho Y, Bae GU, Kim SN, Kim YK.Hwang JW, et al.Exp Mol Med. 2021 May;53(5):788-808. doi: 10.1038/s12276-021-00613-y. Epub 2021 May 18.Exp Mol Med. 2021.PMID: 34006904Free PMC article.Review. 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